› 5usf

X-ray diffraction
2.75Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-230593 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
tyrosine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 686 amino acids
Theoretical weight: 75.34 KDa
Source organism: Leishmania donovani BPK282A1
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A3Q8ID88 (Residues: 1-682; Coverage: 100%)
Gene names: CGC21_5135, LDBPK_141460, LdCL_140020400
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:
Immunoglobulin heavy chain variable region Chains: C, D
Molecule details ›
Chains: C, D
Length: 128 amino acids
Theoretical weight: 14.21 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand YSA 2 x YSA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P65
Unit cell:
a: 96.18Å b: 96.18Å c: 351.83Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.189 0.244
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Associations between Neurological Diseases and Mutations in the Human Glycyl-tRNA Synthetase.
Vinogradova et al. (2021)
2 more

2 mentions without citation

Aminoacyl tRNA synthetases as malarial drug targets: a comparative bioinformatics study.
Nyamai et al. (2019)
1 more